Abstract
Metal selectivity in P1B-type ATPase transporters is determined by conserved amino acid residues in their transmembrane helices responsible for metal binding and transport across the cellular membrane. The Cu(2+)-selective CopB from Archaeoglobus fulgidus has been investigated to explore the coordination chemistry of the transition metal binding sites in P1B-3-type ATPases. Electronic absorption, electron paramagnetic resonance, and X-ray absorption spectroscopic studies indicate the presence of a high-affinity transmembrane Type-2-like Cu(2+) center in which a single cupric ion is coordinated in a distorted square pyramidal geometry by mixed nitrogen/oxygen and sulfur ligands.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Adenosine Triphosphatases / chemistry*
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Adenosine Triphosphatases / metabolism*
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Archaeal Proteins / chemistry*
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Archaeal Proteins / metabolism*
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Archaeoglobus fulgidus / chemistry
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Archaeoglobus fulgidus / enzymology*
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Archaeoglobus fulgidus / metabolism
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Binding Sites
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Cation Transport Proteins / chemistry*
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Cation Transport Proteins / metabolism*
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Copper / metabolism*
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Copper Transport Proteins
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Electron Spin Resonance Spectroscopy
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Metals / metabolism
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Protein Conformation
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X-Ray Absorption Spectroscopy
Substances
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Archaeal Proteins
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Cation Transport Proteins
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CopB protein, Archaea
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Copper Transport Proteins
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Metals
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Copper
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Adenosine Triphosphatases